Fluorine in PDB 6opj: Menin in Complex with Peptide Inhibitor 25

The structure of Menin in Complex with Peptide Inhibitor 25, PDB code: 6opj was solved by B.M.Linhares, P.Fortuna, T.Cierpicki, J.Grembecka, L.Berlicki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.98 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.867, 78.145, 123.702, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 19.7

The binding sites of Fluorine atom in the Menin in Complex with Peptide Inhibitor 25 (pdb code 6opj). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Menin in Complex with Peptide Inhibitor 25, PDB code: 6opj:

Fluorine binding site 1 out of 1 in the Menin in Complex with Peptide Inhibitor 25


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Menin in Complex with Peptide Inhibitor 25 within 5.0Å range: probe atom residue distance (Å) B Occ B:F6 b:24.8 occ:1.00 FAK B:N0A6 0.0 24.8 1.0 CAG B:N0A6 1.4 18.6 1.0 CD1 B:N0A6 2.3 16.0 1.0 CAH B:N0A6 2.5 19.6 1.0 C A:HIS181 2.9 13.8 1.0 N A:ALA182 3.0 14.2 1.0 CA A:HIS181 3.1 13.6 1.0 CB A:SER155 3.2 17.1 1.0 CB A:ALA182 3.3 14.8 1.0 O A:HIS181 3.5 14.7 1.0 N A:HIS181 3.5 13.5 1.0 CA A:ALA182 3.7 13.4 1.0 CG B:N0A6 3.7 14.8 1.0 CAI B:N0A6 3.7 19.2 1.0 O A:HOH720 3.7 28.5 1.0 C A:ASP180 4.0 13.9 1.0 CA A:SER155 4.0 14.4 1.0 O A:ASP180 4.1 16.1 1.0 OG A:SER155 4.1 15.6 1.0 CD2 B:N0A6 4.2 15.8 1.0 CB A:HIS181 4.5 13.4 1.0 N A:SER155 4.6 15.4 1.0 O A:HOH816 4.6 31.4 1.0 ND1 A:HIS181 4.6 18.1 1.0 CB B:N0A6 4.9 15.6 1.0 CD B:PRO7 4.9 14.0 1.0 CD2 A:LEU177 4.9 15.7 1.0 C A:ALA182 4.9 14.4 1.0 CG A:HIS181 5.0 15.1 1.0

P.Fortuna, B.M.Linhares, T.Purohit, J.Pollock, T.Cierpicki, J.Grembecka, L.Berlicki. Covalent and Noncovalent Constraints Yield A Figure Eight-Like Conformation of A Peptide Inhibiting the Menin-Mll Interaction. Eur.J.Med.Chem. V. 207 12748 2020.
ISSN: ISSN 0223-5234
PubMed: 32882610
DOI: 10.1016/J.EJMECH.2020.112748